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Details
Link-It Detail - PubMed - 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.
Debug Stats
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PubMed (1)
14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization. 20642453
Genes (11)

Species:
human : 11
SpeciesGeneGeneIdGene NameEvidence
HumanLRRK2120892leucine-rich repeat kinase 2
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanCDC3711140cell division cycle 37
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanYWHAQ10971tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta polypeptide
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanYWHAZ7534tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta polypeptide
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanYWHAH7533tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, eta polypeptide
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanYWHAG7532tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanYWHAE7531tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanYWHAB7529tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanMARK34140MAP/microtubule affinity-regulating kinase 3
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanHSP90AB13326heat shock protein 90kDa alpha (cytosolic), class B member 1
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
HumanHSP90AA13320heat shock protein 90kDa alpha (cytosolic), class A member 1
PUBMED, Pubmed Id: 20642453, PUBMED ID: 20642453
XRefs (1)

XRef Types:
pubmed : 1


ToppGene Datasets:
none : 1
ToppGene DatasetsXRef TypeXRef IdXRefValuesSourceTop % Rank
PUBMEDimg 2064245314-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.0self